Chiral deaza-coelenterazine analogs for probing a substrate-binding site in the Ca2+-binding photoprotein aequorin
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چکیده
منابع مشابه
Site-specific mutagenesis of the calcium-binding photoprotein aequorin.
The luminescent protein aequorin from the jellyfish Aequoria victoria emits light by an intramolecular reaction in the presence of a trace amount of Ca(2+). In order to understand the mechanism of the reaction, a study of structure-function relationships was undertaken with respect to modifying certain of its amino acid residues. This was done by carrying out oligonucleotide-directed site-speci...
متن کاملPeroxidized coelenterazine, the active group in the photoprotein aequorin.
The photoprotein aequorin emits light by an intramolecular reaction when Ca2+ is added under either aerobic or anaerobic conditions. Previously reported evidence has indicated two possibilities: (i) the functional group of aequorin is coelenterazine itself, a compond that plays key roles in the bioluminescence of various other types of organisms, or (ii) it is the enolized form of this compound...
متن کاملThe binding of substrate analogs to phosphotriesterase.
Phosphotriesterase (PTE) from Pseudomonas diminuta catalyzes the detoxification of organophosphates such as the widely utilized insecticide paraoxon and the chemical warfare agent sarin. The three-dimensional structure of the enzyme is known from high resolution x-ray crystallographic analyses. Each subunit of the homodimer folds into a so-called TIM barrel, with eight strands of parallel beta-...
متن کاملBioluminescence of the Ca(2+)-binding photoprotein, aequorin, after histidine modification.
Modification studies of the 5 histidine residues in aequorin employing site-directed mutagenesis and diethyl pyrocarbonate suggested that His169 may be the site of binding of molecular oxygen in aequorin. The modification of this residue led to complete loss of activity, whereas modification of the remaining 4 histidine residues yielded mutant aequorins with varying bioluminescence activities.
متن کاملProbing the substrate binding site of Candida tenuis xylose reductase (AKR2B5) with site-directed mutagenesis.
Little is known about how substrates bind to CtXR (Candida tenuis xylose reductase; AKR2B5) and other members of the AKR (aldo-keto reductase) protein superfamily. Modelling of xylose into the active site of CtXR suggested that Trp23, Asp50 and Asn309 are the main components of pentose-specific substrate-binding recognition. Kinetic consequences of site-directed substitutions of these residues ...
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ژورنال
عنوان ژورنال: PLOS ONE
سال: 2021
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0251743